Difference between revisions of "Part:BBa K3722004"
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===Biology=== | ===Biology=== | ||
Two flexible linkers and one rigid linker were compared, considering that the linker may affect substrate diffusion to the active site pocket or the flexibility of such linkers may reduce activity[1]. Finally found that the chimeric enzymes showed highly increased ratios of their soluble forms in E. coli. The molar concentrations of soluble Fre-Linker–SttH was 1.64 μM, which was more than 3 times higher than that of SttH by itself[2]. | Two flexible linkers and one rigid linker were compared, considering that the linker may affect substrate diffusion to the active site pocket or the flexibility of such linkers may reduce activity[1]. Finally found that the chimeric enzymes showed highly increased ratios of their soluble forms in E. coli. The molar concentrations of soluble Fre-Linker–SttH was 1.64 μM, which was more than 3 times higher than that of SttH by itself[2]. | ||
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===Usage=== | ===Usage=== | ||
The part was used to construct SttH and Fre fusion enzyme to enhance the solubility and activity of SttH. Due to the limited time, we did not characterize this part. As a result, there is a lack of data about this part. | The part was used to construct SttH and Fre fusion enzyme to enhance the solubility and activity of SttH. Due to the limited time, we did not characterize this part. As a result, there is a lack of data about this part. | ||
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===References=== | ===References=== | ||
Revision as of 05:20, 21 October 2021
A linker sequence in fusion protein Fre-Linker-SttH
A linker sequence belongs to our fusion protein Fre-Linker-SttH, coding a rigid linker between Fre and SttH.
Biology
Two flexible linkers and one rigid linker were compared, considering that the linker may affect substrate diffusion to the active site pocket or the flexibility of such linkers may reduce activity[1]. Finally found that the chimeric enzymes showed highly increased ratios of their soluble forms in E. coli. The molar concentrations of soluble Fre-Linker–SttH was 1.64 μM, which was more than 3 times higher than that of SttH by itself[2].
Usage
The part was used to construct SttH and Fre fusion enzyme to enhance the solubility and activity of SttH. Due to the limited time, we did not characterize this part. As a result, there is a lack of data about this part.
References
[1] Aalbers, F . S. & Fraaije, M. W . Coupled reactions by coupled enzymes: alcohol to lactone cascade with alcohol dehydrogenase-cyclohexanone monooxygenase fusions. Appl. Microbiol. Biotechnol. 101, 7557–7565 (2017). [2] Lee, J., Kim, J., Song, J.E. et al. Production of Tyrian purple indigoid dye from tryptophan in Escherichia coli. Nat Chem Biol 17, 104–112 (2021). https://doi.org/10.1038/s41589-020-00684-4
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]